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{{Infobox_gene}}
{{PBB_Controls
'''Amyloid beta A4 precursor protein-binding family A member 1''' is a [[protein]] that in humans is encoded by the ''APBA1'' [[gene]].<ref name="pmid7678331">{{cite journal | vauthors = Duclos F, Boschert U, Sirugo G, Mandel JL, Hen R, Koenig M | title = Gene in the region of the Friedreich ataxia locus encodes a putative transmembrane protein expressed in the nervous system | journal = Proc Natl Acad Sci U S A | volume = 90 | issue = 1 | pages = 109–13 | date = February 1993 | pmid = 7678331 | pmc = 45609 | doi = 10.1073/pnas.90.1.109 }}</ref><ref name="pmid7719031">{{cite journal | vauthors = Duclos F, Koenig M | title = Comparison of primary structure of a neuron-specific protein, X11, between human and mouse | journal = Mamm Genome | volume = 6 | issue = 1 | pages = 57–8 | date = May 1995 | pmid = 7719031 | pmc = | doi = 10.1007/BF00350899 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: APBA1 amyloid beta (A4) precursor protein-binding, family A, member 1 (X11)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=320| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_APBA1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aqc.
| PDB = {{PDB2|1aqc}}, {{PDB2|1u37}}, {{PDB2|1u38}}, {{PDB2|1u39}}, {{PDB2|1u3b}}, {{PDB2|1x11}}, {{PDB2|1x45}}, {{PDB2|1y7n}}
| Name = Amyloid beta (A4) precursor protein-binding, family A, member 1 (X11)
| HGNCid = 578
| Symbol = APBA1
| AltSymbols =; D9S411E; MINT1; X11; X11A; X11ALPHA
| OMIM = 602414
| ECnumber = 
| Homologene = 897
| MGIid = 1860297
| GeneAtlas_image1 = PBB_GE_APBA1_206679_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0008021 |text = synaptic vesicle}}
| Process = {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0006886 |text = intracellular protein transport}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0008088 |text = axon cargo transport}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 320
    | Hs_Ensembl = ENSG00000107282
    | Hs_RefseqProtein = NP_001154
    | Hs_RefseqmRNA = NM_001163
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 9
    | Hs_GenLoc_start = 71235022
    | Hs_GenLoc_end = 71477042
    | Hs_Uniprot = Q02410
    | Mm_EntrezGene = 319924
    | Mm_Ensembl = ENSMUSG00000024897
    | Mm_RefseqmRNA = NM_177034
    | Mm_RefseqProtein = NP_796008
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 23825973
    | Mm_GenLoc_end = 24016694
    | Mm_Uniprot = 
  }}
}}
'''Amyloid beta (A4) precursor protein-binding, family A, member 1 (X11)''', also known as '''APBA1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: APBA1 amyloid beta (A4) precursor protein-binding, family A, member 1 (X11)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=320| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The protein encoded by this gene is a member of the X11 protein family. It is a neuronal adaptor protein that interacts with the Alzheimer's disease [[amyloid precursor protein]] (APP). It stabilises APP and inhibits production of proteolytic APP fragments including the A beta peptide that is deposited in the brains of [[Alzheimer's disease]] patients. This gene product is believed to be involved in signal transduction processes. It is also regarded as a putative vesicular trafficking protein in the brain that can form a complex with the potential to couple synaptic vesicle exocytosis to neuronal cell adhesion.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the X11 protein family. It is a neuronal adaptor protein that interacts with the Alzheimer's disease amyloid precursor protein (APP). It stabilises APP and inhibits production of proteolytic APP fragments including the A beta peptide that is deposited in the brains of Alzheimer's disease patients. This gene product is believed to be involved in signal transduction processes. It is also regarded as a putative vesicular trafficking protein in the brain that can form a complex with the potential to couple synaptic vesicle exocytosis to neuronal cell adhesion.<ref name="entrez">{{cite web | title = Entrez Gene: APBA1 amyloid beta (A4) precursor protein-binding, family A, member 1 (X11)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=320| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=van der Geer P, Pawson T |title=The PTB domain: a new protein module implicated in signal transduction. |journal=Trends Biochem. Sci. |volume=20 |issue= 7 |pages= 277-80 |year= 1995 |pmid= 7545337 |doi=  }}
*{{cite journal  | author=Chen WJ, Goldstein JL, Brown MS |title=NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor. |journal=J. Biol. Chem. |volume=265 |issue= 6 |pages= 3116-23 |year= 1990 |pmid= 1968060 |doi=  }}
*{{cite journal  | author=Duclos F, Boschert U, Sirugo G, ''et al.'' |title=Gene in the region of the Friedreich ataxia locus encodes a putative transmembrane protein expressed in the nervous system. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 1 |pages= 109-13 |year= 1993 |pmid= 7678331 |doi=  }}
*{{cite journal  | author=Duclos F, Koenig M |title=Comparison of primary structure of a neuron-specific protein, X11, between human and mouse. |journal=Mamm. Genome |volume=6 |issue= 1 |pages= 57-8 |year= 1995 |pmid= 7719031 |doi=  }}
*{{cite journal  | author=Borg JP, Ooi J, Levy E, Margolis B |title=The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. |journal=Mol. Cell. Biol. |volume=16 |issue= 11 |pages= 6229-41 |year= 1996 |pmid= 8887653 |doi=  }}
*{{cite journal  | author=Zhang Z, Lee CH, Mandiyan V, ''et al.'' |title=Sequence-specific recognition of the internalization motif of the Alzheimer's amyloid precursor protein by the X11 PTB domain. |journal=EMBO J. |volume=16 |issue= 20 |pages= 6141-50 |year= 1997 |pmid= 9321393 |doi= 10.1093/emboj/16.20.6141 }}
*{{cite journal  | author=Okamoto M, Südhof TC |title=Mints, Munc18-interacting proteins in synaptic vesicle exocytosis. |journal=J. Biol. Chem. |volume=272 |issue= 50 |pages= 31459-64 |year= 1998 |pmid= 9395480 |doi=  }}
*{{cite journal  | author=Blanco G, Irving NG, Brown SD, ''et al.'' |title=Mapping of the human and murine X11-like genes (APBA2 and apba2), the murine Fe65 gene (Apbb1), and the human Fe65-like gene (APBB2): genes encoding phosphotyrosine-binding domain proteins that interact with the Alzheimer's disease amyloid precursor protein. |journal=Mamm. Genome |volume=9 |issue= 6 |pages= 473-5 |year= 1998 |pmid= 9585438 |doi=  }}
*{{cite journal  | author=Borg JP, Yang Y, De Taddéo-Borg M, ''et al.'' |title=The X11alpha protein slows cellular amyloid precursor protein processing and reduces Abeta40 and Abeta42 secretion. |journal=J. Biol. Chem. |volume=273 |issue= 24 |pages= 14761-6 |year= 1998 |pmid= 9614075 |doi=  }}
*{{cite journal  | author=Butz S, Okamoto M, Südhof TC |title=A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. |journal=Cell |volume=94 |issue= 6 |pages= 773-82 |year= 1998 |pmid= 9753324 |doi=  }}
*{{cite journal  | author=Borg JP, Straight SW, Kaech SM, ''et al.'' |title=Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting. |journal=J. Biol. Chem. |volume=273 |issue= 48 |pages= 31633-6 |year= 1998 |pmid= 9822620 |doi=  }}
*{{cite journal  | author=Borg JP, Lõpez-Figueroa MO, de Taddèo-Borg M, ''et al.'' |title=Molecular analysis of the X11-mLin-2/CASK complex in brain. |journal=J. Neurosci. |volume=19 |issue= 4 |pages= 1307-16 |year= 1999 |pmid= 9952408 |doi=  }}
*{{cite journal  | author=Maximov A, Südhof TC, Bezprozvanny I |title=Association of neuronal calcium channels with modular adaptor proteins. |journal=J. Biol. Chem. |volume=274 |issue= 35 |pages= 24453-6 |year= 1999 |pmid= 10455105 |doi=  }}
*{{cite journal  | author=Mueller HT, Borg JP, Margolis B, Turner RS |title=Modulation of amyloid precursor protein metabolism by X11alpha /Mint-1. A deletion analysis of protein-protein interaction domains. |journal=J. Biol. Chem. |volume=275 |issue= 50 |pages= 39302-6 |year= 2001 |pmid= 11010978 |doi= 10.1074/jbc.M008453200 }}
*{{cite journal  | author=Biederer T, Südhof TC |title=Mints as adaptors. Direct binding to neurexins and recruitment of munc18. |journal=J. Biol. Chem. |volume=275 |issue= 51 |pages= 39803-6 |year= 2001 |pmid= 11036064 |doi= 10.1074/jbc.C000656200 }}
*{{cite journal  | author=Lau KF, McLoughlin DM, Standen C, Miller CC |title=X11 alpha and x11 beta interact with presenilin-1 via their PDZ domains. |journal=Mol. Cell. Neurosci. |volume=16 |issue= 5 |pages= 557-65 |year= 2001 |pmid= 11083918 |doi= 10.1006/mcne.2000.0898 }}
*{{cite journal  | author=McLoughlin DM, Standen CL, Lau KF, ''et al.'' |title=The neuronal adaptor protein X11alpha interacts with the copper chaperone for SOD1 and regulates SOD1 activity. |journal=J. Biol. Chem. |volume=276 |issue= 12 |pages= 9303-7 |year= 2001 |pmid= 11115513 |doi= 10.1074/jbc.M010023200 }}
*{{cite journal  | author=Bécamel C, Alonso G, Galéotti N, ''et al.'' |title=Synaptic multiprotein complexes associated with 5-HT(2C) receptors: a proteomic approach. |journal=EMBO J. |volume=21 |issue= 10 |pages= 2332-42 |year= 2002 |pmid= 12006486 |doi= 10.1093/emboj/21.10.2332 }}
*{{cite journal  | author=Ho CS, Marinescu V, Steinhilb ML, ''et al.'' |title=Synergistic effects of Munc18a and X11 proteins on amyloid precursor protein metabolism. |journal=J. Biol. Chem. |volume=277 |issue= 30 |pages= 27021-8 |year= 2002 |pmid= 12016213 |doi= 10.1074/jbc.M201823200 }}
}}
{{refend}}


{{protein-stub}}
APBA1 has been shown to [[Protein-protein interaction|interact]] with [[KCNJ12]],<ref name=pmid15024025>{{cite journal | vauthors = Leonoudakis D, Conti LR, Anderson S, Radeke CM, McGuire LM, Adams ME, Froehner SC, Yates JR, Vandenberg CA | title = Protein trafficking and anchoring complexes revealed by proteomic analysis of inward rectifier potassium channel (Kir2.x)-associated proteins | journal = J. Biol. Chem. | volume = 279 | issue = 21 | pages = 22331–46 | date = May 2004 | pmid = 15024025 | doi = 10.1074/jbc.M400285200 }}</ref><ref name=pmid14960569>{{cite journal | vauthors = Leonoudakis D, Conti LR, Radeke CM, McGuire LM, Vandenberg CA | title = A multiprotein trafficking complex composed of SAP97, CASK, Veli, and Mint1 is associated with inward rectifier Kir2 potassium channels | journal = J. Biol. Chem. | volume = 279 | issue = 18 | pages = 19051–63 | date = April 2004 | pmid = 14960569 | doi = 10.1074/jbc.M400284200 }}</ref> [[CCS (gene)|CCS]],<ref name=pmid11115513>{{cite journal | vauthors = McLoughlin DM, Standen CL, Lau KF, Ackerley S, Bartnikas TP, Gitlin JD, Miller CC | title = The neuronal adaptor protein X11alpha interacts with the copper chaperone for SOD1 and regulates SOD1 activity | journal = J. Biol. Chem. | volume = 276 | issue = 12 | pages = 9303–7 | date = March 2001 | pmid = 11115513 | doi = 10.1074/jbc.M010023200 }}</ref> [[CASK]]<ref name=pmid9822620>{{cite journal | vauthors = Borg JP, Straight SW, Kaech SM, de Taddéo-Borg M, Kroon DE, Karnak D, Turner RS, Kim SK, Margolis B | title = Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting | journal = J. Biol. Chem. | volume = 273 | issue = 48 | pages = 31633–6 | date = November 1998 | pmid = 9822620 | doi = 10.1074/jbc.273.48.31633 }}</ref><ref name=pmid9952408>{{cite journal | vauthors = Borg JP, Lõpez-Figueroa MO, de Taddèo-Borg M, Kroon DE, Turner RS, Watson SJ, Margolis B | title = Molecular analysis of the X11-mLin-2/CASK complex in brain | journal = J. Neurosci. | volume = 19 | issue = 4 | pages = 1307–16 | date = February 1999 | pmid = 9952408 }}</ref> and [[Amyloid precursor protein]].<ref name=pmid12196555>{{cite journal | vauthors = Biederer T, Cao X, Südhof TC, Liu X | title = Regulation of APP-dependent transcription complexes by Mint/X11s: differential functions of Mint isoforms | journal = J. Neurosci. | volume = 22 | issue = 17 | pages = 7340–51 | date = September 2002 | pmid = 12196555 }}</ref><ref name=pmid8887653>{{cite journal | vauthors = Borg JP, Ooi J, Levy E, Margolis B | title = The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein | journal = Mol. Cell. Biol. | volume = 16 | issue = 11 | pages = 6229–41 | date = November 1996 | pmid = 8887653 | pmc = 231626 | doi=10.1128/mcb.16.11.6229}}</ref>
{{WikiDoc Sources}}
 
== References ==
{{Reflist}}
 
== Further reading ==
{{Refbegin | 2}}
* {{cite journal | vauthors = van der Geer P, Pawson T | title = The PTB domain: a new protein module implicated in signal transduction. | journal = Trends Biochem. Sci. | volume = 20 | issue = 7 | pages = 277–80 | year = 1995 | pmid = 7545337 | doi = 10.1016/S0968-0004(00)89043-X }}
* {{cite journal | vauthors = Chen WJ, Goldstein JL, Brown MS | title = NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor. | journal = J. Biol. Chem. | volume = 265 | issue = 6 | pages = 3116–23 | year = 1990 | pmid = 1968060 | doi =  }}
* {{cite journal | vauthors = Borg JP, Ooi J, Levy E, Margolis B | title = The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. | journal = Mol. Cell. Biol. | volume = 16 | issue = 11 | pages = 6229–41 | year = 1996 | pmid = 8887653 | pmc = 231626 | doi =  10.1128/mcb.16.11.6229}}
* {{cite journal | vauthors = Zhang Z, Lee CH, Mandiyan V, Borg JP, Margolis B, Schlessinger J, Kuriyan J | title = Sequence-specific recognition of the internalization motif of the Alzheimer's amyloid precursor protein by the X11 PTB domain. | journal = EMBO J. | volume = 16 | issue = 20 | pages = 6141–50 | year = 1997 | pmid = 9321393 | pmc = 1326298 | doi = 10.1093/emboj/16.20.6141 }}
* {{cite journal | vauthors = Okamoto M, Südhof TC | title = Mints, Munc18-interacting proteins in synaptic vesicle exocytosis. | journal = J. Biol. Chem. | volume = 272 | issue = 50 | pages = 31459–64 | year = 1998 | pmid = 9395480 | doi = 10.1074/jbc.272.50.31459 }}
* {{cite journal | vauthors = Blanco G, Irving NG, Brown SD, Miller CC, McLoughlin DM | title = Mapping of the human and murine X11-like genes (APBA2 and apba2), the murine Fe65 gene (Apbb1), and the human Fe65-like gene (APBB2): genes encoding phosphotyrosine-binding domain proteins that interact with the Alzheimer's disease amyloid precursor protein. | journal = Mamm. Genome | volume = 9 | issue = 6 | pages = 473–5 | year = 1998 | pmid = 9585438 | doi = 10.1007/s003359900800 }}
* {{cite journal | vauthors = Borg JP, Yang Y, De Taddéo-Borg M, Margolis B, Turner RS | title = The X11alpha protein slows cellular amyloid precursor protein processing and reduces Abeta40 and Abeta42 secretion. | journal = J. Biol. Chem. | volume = 273 | issue = 24 | pages = 14761–6 | year = 1998 | pmid = 9614075 | doi = 10.1074/jbc.273.24.14761 }}
* {{cite journal | vauthors = Butz S, Okamoto M, Südhof TC | title = A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. | journal = Cell | volume = 94 | issue = 6 | pages = 773–82 | year = 1998 | pmid = 9753324 | doi = 10.1016/S0092-8674(00)81736-5 }}
* {{cite journal | vauthors = Borg JP, Straight SW, Kaech SM, de Taddéo-Borg M, Kroon DE, Karnak D, Turner RS, Kim SK, Margolis B | title = Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting. | journal = J. Biol. Chem. | volume = 273 | issue = 48 | pages = 31633–6 | year = 1998 | pmid = 9822620 | doi = 10.1074/jbc.273.48.31633 }}
* {{cite journal | vauthors = Borg JP, Lõpez-Figueroa MO, de Taddèo-Borg M, Kroon DE, Turner RS, Watson SJ, Margolis B | title = Molecular analysis of the X11-mLin-2/CASK complex in brain. | journal = J. Neurosci. | volume = 19 | issue = 4 | pages = 1307–16 | year = 1999 | pmid = 9952408 | doi =  }}
* {{cite journal | vauthors = Maximov A, Südhof TC, Bezprozvanny I | title = Association of neuronal calcium channels with modular adaptor proteins. | journal = J. Biol. Chem. | volume = 274 | issue = 35 | pages = 24453–6 | year = 1999 | pmid = 10455105 | doi = 10.1074/jbc.274.35.24453 }}
* {{cite journal | vauthors = Mueller HT, Borg JP, Margolis B, Turner RS | title = Modulation of amyloid precursor protein metabolism by X11alpha /Mint-1. A deletion analysis of protein-protein interaction domains. | journal = J. Biol. Chem. | volume = 275 | issue = 50 | pages = 39302–6 | year = 2001 | pmid = 11010978 | doi = 10.1074/jbc.M008453200 }}
* {{cite journal | vauthors = Biederer T, Südhof TC | title = Mints as adaptors. Direct binding to neurexins and recruitment of munc18. | journal = J. Biol. Chem. | volume = 275 | issue = 51 | pages = 39803–6 | year = 2001 | pmid = 11036064 | doi = 10.1074/jbc.C000656200 }}
* {{cite journal | vauthors = Lau KF, McLoughlin DM, Standen C, Miller CC | title = X11 alpha and x11 beta interact with presenilin-1 via their PDZ domains. | journal = Mol. Cell. Neurosci. | volume = 16 | issue = 5 | pages = 557–65 | year = 2001 | pmid = 11083918 | doi = 10.1006/mcne.2000.0898 }}
* {{cite journal | vauthors = McLoughlin DM, Standen CL, Lau KF, Ackerley S, Bartnikas TP, Gitlin JD, Miller CC | title = The neuronal adaptor protein X11alpha interacts with the copper chaperone for SOD1 and regulates SOD1 activity. | journal = J. Biol. Chem. | volume = 276 | issue = 12 | pages = 9303–7 | year = 2001 | pmid = 11115513 | doi = 10.1074/jbc.M010023200 }}
* {{cite journal | vauthors = Bécamel C, Alonso G, Galéotti N, Demey E, Jouin P, Ullmer C, Dumuis A, Bockaert J, Marin P | title = Synaptic multiprotein complexes associated with 5-HT(2C) receptors: a proteomic approach. | journal = EMBO J. | volume = 21 | issue = 10 | pages = 2332–42 | year = 2002 | pmid = 12006486 | pmc = 126011 | doi = 10.1093/emboj/21.10.2332 }}
* {{cite journal | vauthors = Ho CS, Marinescu V, Steinhilb ML, Gaut JR, Turner RS, Stuenkel EL | title = Synergistic effects of Munc18a and X11 proteins on amyloid precursor protein metabolism. | journal = J. Biol. Chem. | volume = 277 | issue = 30 | pages = 27021–8 | year = 2002 | pmid = 12016213 | doi = 10.1074/jbc.M201823200 }}
{{Refend}}
 
==External links==
* {{UCSC gene info|APBA1}}
{{PDB Gallery|geneid=320}}
 
 
{{Gene-9-stub}}

Latest revision as of 18:06, 29 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Amyloid beta A4 precursor protein-binding family A member 1 is a protein that in humans is encoded by the APBA1 gene.[1][2][3]

Function

The protein encoded by this gene is a member of the X11 protein family. It is a neuronal adaptor protein that interacts with the Alzheimer's disease amyloid precursor protein (APP). It stabilises APP and inhibits production of proteolytic APP fragments including the A beta peptide that is deposited in the brains of Alzheimer's disease patients. This gene product is believed to be involved in signal transduction processes. It is also regarded as a putative vesicular trafficking protein in the brain that can form a complex with the potential to couple synaptic vesicle exocytosis to neuronal cell adhesion.[3]

Interactions

APBA1 has been shown to interact with KCNJ12,[4][5] CCS,[6] CASK[7][8] and Amyloid precursor protein.[9][10]

References

  1. ↑ Duclos F, Boschert U, Sirugo G, Mandel JL, Hen R, Koenig M (February 1993). "Gene in the region of the Friedreich ataxia locus encodes a putative transmembrane protein expressed in the nervous system". Proc Natl Acad Sci U S A. 90 (1): 109–13. doi:10.1073/pnas.90.1.109. PMC 45609. PMID 7678331.
  2. ↑ Duclos F, Koenig M (May 1995). "Comparison of primary structure of a neuron-specific protein, X11, between human and mouse". Mamm Genome. 6 (1): 57–8. doi:10.1007/BF00350899. PMID 7719031.
  3. ↑ 3.0 3.1 "Entrez Gene: APBA1 amyloid beta (A4) precursor protein-binding, family A, member 1 (X11)".
  4. ↑ Leonoudakis D, Conti LR, Anderson S, Radeke CM, McGuire LM, Adams ME, Froehner SC, Yates JR, Vandenberg CA (May 2004). "Protein trafficking and anchoring complexes revealed by proteomic analysis of inward rectifier potassium channel (Kir2.x)-associated proteins". J. Biol. Chem. 279 (21): 22331–46. doi:10.1074/jbc.M400285200. PMID 15024025.
  5. ↑ Leonoudakis D, Conti LR, Radeke CM, McGuire LM, Vandenberg CA (April 2004). "A multiprotein trafficking complex composed of SAP97, CASK, Veli, and Mint1 is associated with inward rectifier Kir2 potassium channels". J. Biol. Chem. 279 (18): 19051–63. doi:10.1074/jbc.M400284200. PMID 14960569.
  6. ↑ McLoughlin DM, Standen CL, Lau KF, Ackerley S, Bartnikas TP, Gitlin JD, Miller CC (March 2001). "The neuronal adaptor protein X11alpha interacts with the copper chaperone for SOD1 and regulates SOD1 activity". J. Biol. Chem. 276 (12): 9303–7. doi:10.1074/jbc.M010023200. PMID 11115513.
  7. ↑ Borg JP, Straight SW, Kaech SM, de Taddéo-Borg M, Kroon DE, Karnak D, Turner RS, Kim SK, Margolis B (November 1998). "Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting". J. Biol. Chem. 273 (48): 31633–6. doi:10.1074/jbc.273.48.31633. PMID 9822620.
  8. ↑ Borg JP, Lõpez-Figueroa MO, de Taddèo-Borg M, Kroon DE, Turner RS, Watson SJ, Margolis B (February 1999). "Molecular analysis of the X11-mLin-2/CASK complex in brain". J. Neurosci. 19 (4): 1307–16. PMID 9952408.
  9. ↑ Biederer T, Cao X, Südhof TC, Liu X (September 2002). "Regulation of APP-dependent transcription complexes by Mint/X11s: differential functions of Mint isoforms". J. Neurosci. 22 (17): 7340–51. PMID 12196555.
  10. ↑ Borg JP, Ooi J, Levy E, Margolis B (November 1996). "The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein". Mol. Cell. Biol. 16 (11): 6229–41. doi:10.1128/mcb.16.11.6229. PMC 231626. PMID 8887653.

Further reading

External links


Retrieved from "https://www.wikidoc.org/index.php?title=APBA1&oldid=1422559"